Research workbench
Crystal structure of unliganded form of guanylate kinase from yeast
Analyse Crystal structure of unliganded form of guanylate kinase from yeast in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EX6
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate kinase
- EC
- 2.7.4.8
- UniProt
- P15454
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Guanylate kinase (EC 2.7.4.8) | protein | 186 | 41% helix, 22% strand | P15454 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.50 | 0.73 | 34 | empty |
| 2 | 50 | 0.31 | 0.76 | 12 | empty |
| 3 | 53 | 0.27 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 239 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P15454
- Elsewhere: RCSB PDB 1EX6 · PDBe 1EX6 · UniProt P15454
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